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Structural basis for the function and inhibition of an influenza virus proton channel

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  • Amanda L. Stouffer

    (School of Medicine
    University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA
    Present addresses: Laboratory of Organic Chemistry, ETH Hönggerberg, 8093 Zurich, Switzerland (A.L.S.); Polgenix, Inc., Cleveland, Ohio 44106, USA (D.S); Box 2525, Brown University, Providence, Rhode Island 02912, USA (A.S.L.); Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Piscataway, New Jersey 08854, USA (V.N.).)

  • Rudresh Acharya

    (School of Medicine)

  • David Salom

    (School of Medicine
    Present addresses: Laboratory of Organic Chemistry, ETH Hönggerberg, 8093 Zurich, Switzerland (A.L.S.); Polgenix, Inc., Cleveland, Ohio 44106, USA (D.S); Box 2525, Brown University, Providence, Rhode Island 02912, USA (A.S.L.); Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Piscataway, New Jersey 08854, USA (V.N.).)

  • Anna S. Levine

    (School of Medicine
    Present addresses: Laboratory of Organic Chemistry, ETH Hönggerberg, 8093 Zurich, Switzerland (A.L.S.); Polgenix, Inc., Cleveland, Ohio 44106, USA (D.S); Box 2525, Brown University, Providence, Rhode Island 02912, USA (A.S.L.); Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Piscataway, New Jersey 08854, USA (V.N.).)

  • Luigi Di Costanzo

    (University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA)

  • Cinque S. Soto

    (School of Medicine)

  • Valentina Tereshko

    (University of Chicago, Chicago, Illinois 60637, USA)

  • Vikas Nanda

    (School of Medicine
    Present addresses: Laboratory of Organic Chemistry, ETH Hönggerberg, 8093 Zurich, Switzerland (A.L.S.); Polgenix, Inc., Cleveland, Ohio 44106, USA (D.S); Box 2525, Brown University, Providence, Rhode Island 02912, USA (A.S.L.); Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Piscataway, New Jersey 08854, USA (V.N.).)

  • Steven Stayrook

    (School of Medicine)

  • William F. DeGrado

    (School of Medicine
    University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA)

Abstract

Influenza changes channels Until recently, the pH-gated proton channel of influenza A virus, M2, was effectively targeted by amantadine-based antivirals, but resistance to these drugs is now widespread. Two groups now present structural studies of M2 proton channel. Jason Schnell and James Chou determine the structure of a 38-residue segment of M2, in complex with rimantadine, by NMR spectroscopy. Amanda Stouffer et al. determined the crystal structure of a 25-residue fragment of M2, with and without amantadine, using X-ray diffraction. Strikingly, the resulting structures suggest two very different mechanisms by which the drug inhibits the channel. The proposed mechanisms are discussed by Christopher Miller in an accompanying News & Views article.

Suggested Citation

  • Amanda L. Stouffer & Rudresh Acharya & David Salom & Anna S. Levine & Luigi Di Costanzo & Cinque S. Soto & Valentina Tereshko & Vikas Nanda & Steven Stayrook & William F. DeGrado, 2008. "Structural basis for the function and inhibition of an influenza virus proton channel," Nature, Nature, vol. 451(7178), pages 596-599, January.
    • Handle: RePEc:nat:nature:v:451:y:2008:i:7178:d:10.1038_nature06528
    DOI: 10.1038/nature06528
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    Cited by:

    1. Mattia L DiFrancesco & Ulf-Peter Hansen & Gerhard Thiel & Anna Moroni & Indra Schroeder, 2014. "Effect of Cytosolic pH on Inward Currents Reveals Structural Characteristics of the Proton Transport Cycle in the Influenza A Protein M2 in Cell-Free Membrane Patches of Xenopus oocytes," PLOS ONE, Public Library of Science, vol. 9(9), pages 1-12, September.

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